Parasitic protozoa are responsible for a wide variety of infections in man and animals. Many of the diseases are life threatening to the host, and in animal husbandry, can cause considerable economic loss. For example, malaria remains a significant health threat to humans despite massive international attempts to eradicate the disease; trypanosomiasis such as Chagas disease caused by Trypanosoma cruzi and African sleeping sickness caused by T. brucei are not uncommon in South America and Africa, respectively; and opportunistic infections in immunocompromised hosts caused by Pneumocystis carinii, Toxoplasma gondii, Cryptosporidium sp. are becoming increasingly significant in the developed countries.
Coccidiosis, a widespread disease of domesticated animals, is caused by protozoal infection. In the poultry industry, coccidiosis is responsible for high levels of morbidity and mortality in the bird population and may result in extreme economic losses. The infectious agents are protozoa of the genus Eimeria. Some of the most significant avian Eimeria species include E. tenella, E. acervulina, E. necatrix, E. brunetti and E. maxima. 
In some protozoal diseases, such as Chagas disease, there is no satisfactory treatment; in others, drug-resistant strains of the protozoa may develop. Accordingly, there exists a continued need to identify new and effective anti-protozoal drugs. However, antiparasitic drug discovery has been, for the most part, a random and laborious process through biological screening of natural products and synthetic compounds against a panel of parasites. This process can be greatly facilitated and made more specific if a biochemical target of antiprotozoal drugs can be identified, and incorporated into the screening process.
cGMP dependent protein kinases (PKG) catalyze the phosphorylation of specific protein substrates. In the absence of cGMP the activity of these enzymes is very low. In mammalian cells there are two types of PKG, a soluble (PKG1) and a membrane bound form (PKG2). Multiple splice variants of the soluble protein have been identified. PKGs are known to control many cellular processes in higher animals. Mammalian PKG1 is most abundant in smooth muscle, platelets and cerebellum. Targeted disruption of PKG1 in mice generated phenotypes clearly associated with smooth muscle, namely severe intestinal and vascular dysfunctions. PKG2 expression is highest in the small intestine, several regions of the brain (particularly the hypothalamus) and lung. Transgenic mice lacking PKG2 display a dwarfed phenotype caused by defects in ossification at the growth plates and also have intestinal secretion dysfunctions. PKGs have also been identified in Dictyostelium, Paramecium, Tetrahymena and Ascaris. 